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Mass-spectrometric exploration of proteome structure and function

Nature volume 537, pages 347–355 (2016)Cite this article

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Abstract

Numerous biological processes are concurrently and coordinately active in every living cell. Each of them encompasses synthetic, catalytic and regulatory functions that are, almost always, carried out by proteins organized further into higher-order structures and networks. For decades, the structures and functions of selected proteins have been studied using biochemical and biophysical methods. However, the properties and behaviour of the proteome as an integrated system have largely remained elusive. Powerful mass-spectrometry-based technologies now provide unprecedented insights into the composition, structure, function and control of the proteome, shedding light on complex biological processes and phenotypes.

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Figure 1: Bottom-up proteomics workflows.
Figure 2: Analysis of post-translational modifications.
Figure 3: Interaction proteomics and structural proteomics.
Figure 4: Proteotype states and phenotypes.

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Acknowledgements

We thank M. Faini and R. Ciuffa for help in preparing the figures and Y. Liu for help in compiling the literature citations. M. Hein provided inspiration for this Review, read the manuscript critically and helped with preparing the figures, as did F. Hosp, P. Geyer and S. Beck. We thank members of our groups for critical discussions.

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Authors and Affiliations

  1. Department of Biology, Institute of Molecular Systems Biology, ETH Zürich, Zürich, 8093, Switzerland

    Ruedi Aebersold

  2. Faculty of Science, University of Zürich, Zürich, 8093, Switzerland

    Ruedi Aebersold

  3. Department of Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Martinsried, 82152, Germany

    Matthias Mann

  4. Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, 2200, Denmark

    Matthias Mann

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Aebersold, R., Mann, M. Mass-spectrometric exploration of proteome structure and function. Nature 537, 347–355 (2016). https://doi.org/10.1038/nature19949

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  • DOI: https://doi.org/10.1038/nature19949

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